1. Glycoproteomic characterization of recombinant mouse α-dystroglycan.
- Author
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Harrison, Rebecca, Hitchen, Paul G, Panico, Maria, Morris, Howard R, Mekhaiel, David, Pleass, Richard J, Dell, Anne, Hewitt, Jane E, and Haslam, Stuart M
- Subjects
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PROTEOMICS , *LABORATORY mice , *DYSTROGLYCAN , *DYSTROPHIN , *GLYCOPROTEINS , *GLYCOSYLATION , *GALACTOSAMINE , *MASS spectrometry - Abstract
α-Dystroglycan (DG) is a key component of the dystrophin–glycoprotein complex. Aberrant glycosylation of the protein has been linked to various forms of congenital muscular dystrophy. Unusually α-DG has previously been demonstrated to be modified with both O-N-acetylgalactosamine and O-mannose initiated glycans. In the present study, Fc-tagged recombinant mouse α-DG was expressed and purified from human embryonic kidney 293T cells. α-DG glycopeptides were characterized by glycoproteomic strategies using both nano-liquid chromatography matrix-assisted laser desorption ionization and electrospray tandem mass spectrometry. A total of 14 different peptide sequences and 38 glycopeptides were identified which displayed heterogeneous O-glycosylation. These data provide new insights into the complex domain-specific O-glycosylation of α-DG. [ABSTRACT FROM PUBLISHER]
- Published
- 2012
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